1LNS

Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis

Summary for 1LNS

• Entry DOI: 10.2210/pdb1lns/pdb
• Descriptor: X-PROLYL DIPEPTIDYL AMINOPEPTIDASE (2 entities in total)
• Functional Keywords: alpha beta hydrolase fold, hydrolase
• Biological source: Lactococcus lactis
• Cellular location: Cytoplasm: P22346
• Total number of polymer chains: 1
• Total formula weight: 87800.11

Authors

Rigolet, P.,Mechin, I.,Delage, M.M.,Chich, J.F. (deposition date: 2002-05-03, release date: 2002-11-06, Last modification date: 2024-02-14)

Primary citation

Rigolet, P.,Mechin, I.,Delage, M.M.,Chich, J.F.
The Structural Basis for Catalysis and Specificity of the X-prolyl dipepdidyl aminopeptidase from Lactococcus lactis
Structure, 10:1383-1394, 2002

PubMed Abstract: The X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis is a dimeric enzyme catalyzing the removal of Xaa-Pro dipeptides from the N terminus of peptides. The structure of the enzyme was solved at 2.2 A resolution and provides a model for the peptidase family S15. Each monomer is composed of four domains. The larger one presents an alpha/beta hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization. A C-terminal moiety probably plays a role in the tropism of X-PDAP toward the cellular membrane. These results give new insights for further exploration of the role of the enzymes of the SC clan.

PubMed: 12377124
DOI: 10.1016/S0969-2126(02)00851-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)